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AB71550

Anti-ADAMTS13 antibody

4

(1 Review)

|

(4 Publications)

Rabbit Polyclonal ADAMTS13 antibody. Suitable for WB, IHC-P and reacts with Mouse samples. Cited in 4 publications. Immunogen corresponding to Synthetic Peptide within Human ADAMTS13.

View Alternative Names

C9orf8, UNQ6102/PRO20085, ADAMTS13, A disintegrin and metalloproteinase with thrombospondin motifs 13, ADAM-TS 13, ADAM-TS13, ADAMTS-13, von Willebrand factor-cleaving protease, vWF-CP, vWF-cleaving protease

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse

Applications

IHC-P, WB

applications

Immunogen

Synthetic Peptide within Human ADAMTS13. The exact immunogen used to generate this antibody is proprietary information.

Q76LX8

Specificity

This antibody reacts specifically with human 154 kDa ADAMTS13 protein

Reactivity data

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Properties and storage information

Form
Liquid
Purity
Whole antiserum
Storage buffer
Constituents: Whole serum
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

ADAMTS13 also known as von Willebrand factor-cleaving protease (VWFCP) is a zinc-containing metalloprotease with a molecular mass of approximately 190 kDa. This protein belongs to the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family and exhibits a complex structure with specific domains including a metalloprotease and a disintegrin-like domain. ADAMTS13 is produced mainly in the liver and circulates in the blood plasma. Research shows that it primarily facilitates the cleavage of von Willebrand factor (vWF) a large multimeric protein essential for blood clotting.
Biological function summary

ADAMTS13 plays a role in regulating the size and function of von Willebrand factor (vWF) ensuring proper hemostatic balance. The enzyme prevents the accumulation of ultra-large vWF multimers which can lead to spontaneous platelet aggregation and thrombus formation. Although ADAMTS13 acts independently its function is closely linked to the dynamics of vWF in response to vascular injury. Properly functioning ADAMTS13 aids in maintaining normal blood flow by preventing unnecessary clot formation in the bloodstream.

Pathways

ADAMTS13 is critical in the coagulation and hemostatic pathways. It operates by modulating the activity of vWF which plays an essential role in platelet adhesion and aggregation forming part of the coagulation cascade. A significant relationship exists between ADAMTS13 and vWF in these pathways as the protease controls vWF multimer size directly impacting clot formation. In the context of hemostatic balance ADAMTS13 intersects with factors like thrombin and fibrinogen which further contribute to clotting processes.

ADAMTS13 deficiency or dysfunction is associated with thrombotic thrombocytopenic purpura (TTP) a rare but severe blood disorder. In TTP the reduced activity of ADAMTS13 leads to an over-accumulation of ultra-large vWF multimers resulting in excessive platelet aggregation and microvascular thrombosis. Another related condition is atypical hemolytic uremic syndrome (aHUS) where abnormal ADAMTS13 activity might exacerbate the disease pathology. Both disorders highlight the critical need for balanced ADAMTS13 function in maintaining vascular health and highlight its potential as a therapeutic target.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation.
See full target information ADAMTS13

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

Cells 14: PubMed39851513

2025

ADAMTS13 Improves Endothelial Function and Reduces Inflammation in Diabetic Retinopathy.

Applications

Unspecified application

Species

Unspecified reactive species

Ahmed M Abu El-Asrar,Mohd I Nawaz,Ajmal Ahmad,Mairaj Siddiquei,Eef Allegaert,Lowie Adyns,Lotte Vanbrabant,Priscilla W Gikandi,Gert De Hertogh,Sofie Struyf,Ghislain Opdenakker

Molecules (Basel, Switzerland) 27: PubMed36144730

2022

Differential Expression and Localization of ADAMTS Proteinases in Proliferative Diabetic Retinopathy.

Applications

Unspecified application

Species

Unspecified reactive species

Ahmed M Abu El-Asrar,Mohd Imtiaz Nawaz,Eef Allegaert,Mohammad Mairaj Siddiquei,Ajmal Ahmad,Priscilla Gikandi,Gert De Hertogh,Ghislain Opdenakker

The Journal of thoracic and cardiovascular surgery 147:1634-43 PubMed24139617

2013

Insights into the mechanism(s) of von Willebrand factor degradation during mechanical circulatory support.

Applications

WB

Species

Unspecified reactive species

Carlo R Bartoli,Sujith Dassanayaka,Kenneth R Brittian,Andrew Luckett,Srinivas Sithu,Thorsten Siess,Daniel H Raess,Paul A Spence,Steven C Koenig,Robert D Dowling,Stanley E D'Souza

Blood 115:1640-9 PubMed20032502

2009

An autoantibody epitope comprising residues R660, Y661, and Y665 in the ADAMTS13 spacer domain identifies a binding site for the A2 domain of VWF.

Applications

WB

Species

Human

Wouter Pos,James T B Crawley,Rob Fijnheer,Jan Voorberg,David A Lane,Brenda M Luken
View all publications

Product promise

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